IMMUNOCHEMICAL STUDIES OF HUMAN PITUITARY GROWTH HORMONE

1962 ◽  
Vol 40 (2) ◽  
pp. 311-320 ◽  
Author(s):  
Zvi Laron ◽  
Sara Assa
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Haemagglutination Inhibition ◽  
Rabbit Antiserum ◽  
Human Growth ◽  
Human Albumin ◽  
Agar Gel ◽  
Human Pituitary ◽  
Pituitary Glands ◽  
Fraction I

ABSTRACT Human growth hormone (HGH) prepared from human pituitary glands by the method of Raben (1959) showed two components on agar gel electrophoresis. Fraction I corresponded to a slow alpha-globulin, and fraction II had a mobility between alpha and beta-globulin. On agar gel immunoelectrophoresis using HGH and rabbit antiserum to HGH, these two components showed immunological identity. By using agar gel immunoelectrophoresis and the haemagglutination technique HGH preparations of both Raben and Li type were shown to be contaminated with human albumin. Antiserum to human growth hormone containing also antibodies against human albumin was purified by adsorption with human albumin. It is postulated that part of the difficulties encountered in the use of the haemagglutination-inhibition technique to determine growth hormone concentration in serum, is due to impurities in the human growth hormone preparations and antisera to these preparations in use.

IMMUNOCHEMICAL STUDIES ON THE HETEROGENEITY OF HUMAN GROWTH HORMONE (HGH)

1969 ◽  
Vol 60 (1) ◽  
pp. 101-111 ◽  
Author(s):  
W. Rohde ◽  
G. Dörner
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Extraction Procedure ◽  
Gel Filtration ◽  
Human Growth ◽  
Double Diffusion ◽  
Active Components ◽  
Agar Gel ◽  
Human Pituitary ◽  
Starch Gel

ABSTRACT The specific antigenic patterns of human growth hormone in various human pituitary extracts were determined by analysis in gel filtration, in starch gel and agar gel immunoelectrophoresis. The analysis of pituitary extracts by gel filtration on Sephadex G-200 indicates that HGH complexes with different molecular weights were present in all tested pituitary extracts. The rate of formation of high molecular HGH was dependent on the extraction procedure used. Altogether seven immunologically active components of HGH were detected by analysis of crude pituitary extracts in starch gel immunoelectrophoresis. The number and the rate of formed HGH components were dependent on the solvent used for the extraction of pituitary homogenates and on the sequence of extraction procedures. The electrophoretical patterns obtained were reproducible. The electrophoretical behaviour of HGH of various pituitary extracts in agar gel also suggested the presence of multiple components. Three different positions were observed between the α1- and β1-globulins. The analysis of pituitary extracts in the two dimensional double diffusion technique in agar gel using an absorbed anti-HGH-serum gave evidence of the antigenic homogeneity of HGH in the different preparations. It is concluded that the electrophoretic heterogeneity of pituitary growth hormone preparations is already determined by the first step of the extraction.

Using human growth hormone (somatropin)

1989 ◽  
Vol 27 (25) ◽  
pp. 97-98
Keyword(s):  
Growth Hormone ◽  
Young Adults ◽  
Short Stature ◽  
Human Growth Hormone ◽  
Gh Deficiency ◽  
Human Growth ◽  
Turner’S Syndrome ◽  
Human Pituitary ◽  
Pituitary Glands ◽  
Jakob Disease

Short stature was first treated in 1958 with growth hormone (GH) made from human pituitary glands.1 In 1985 biosynthetic GH was introduced after several young adults treated with GH in childhood had died from Creutzfeldt-Jakob disease.2 The first biosynthetic GH somatrem (Somatonorm - KabiVitrum) contains an additional methionyl residue and is licensed for treating short stature of Turner’s syndrome as well as GH deficiency. A preparation identical to human GH is now available (somatropin (rbe); Genotropin - KabiVitrum). Who should have it?

RADIOIMMUNOASSAY STUDIES WITH HUMAN GROWTH HORMONE AND A PITUITARY LIPID MOBILIZING FACTOR

1968 ◽  
Vol 58 (2) ◽  
pp. 318-338 ◽  
Author(s):  
N. Norman ◽  
Aa. R. Turter
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Antibody Formation ◽  
Human Growth ◽  
Structural Features ◽  
The Other ◽  
Human Pituitary ◽  
Pituitary Glands ◽  
Growth Promoting ◽  
The One

ABSTRACT A description is given of a radioimmunoassay procedure for human growth hormone (HGH). Particular emphasis is placed on problems encountered with aggregation and unspecific serum protein binding of the 125I radioiodinated HGH. Immunization of rabbits and guinea pigs with a highly purified lipid mobilizing factor (LMF) from human pituitary glands was attempted. This did not result in antibody formation towards LMF, but gave high titers against HGH. The observation thus suggests that LMF may have structural features in common with the HGH molecule. The antibody towards HGH may, however, also have been produced by a minimal contamination with HGH in the LMF. It was shown that detectable antibody formation towards HGH could be produced in rabbits with as little as 5 μg HGH. During the study of two highly purified HGH preparations – the one containing only growth promoting or somatotrophic activity, the other had adipokinetic activity as well - it was shown that the employed radioimmunoassay is specifically directed against the growth promoting part of HGH. Changes in the serum concentration of a possible physiologically acting LMF could therefore not be recorded, neither by a direct assay nor indirectly. On the other hand, the specificity of the HGH assay towards the »somatotrophin proper« assures that it is indeed this hormone that varies in concentration in response to insulin hypoglycaemia, exercise and postprandially. The stress of acute cardiac infarction did not increase growth hormone in the blood.

Human growth hormone peptide 1?43: Isolation from pituitary glands

1983 ◽  
Vol 2 (6) ◽  
pp. 425-436 ◽  
Author(s):  
Rama N. P. Singh ◽  
Boyd K. Seavey ◽  
Loraine J. Lewis ◽  
Urban J. Lewis
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Pituitary Glands

EFFECT OF HEAT ON THE IMMUNOLOGICAL PROPERTIES OF HUMAN, BOVINE AND OVINE GROWTH HORMONE

1964 ◽  
Vol 46 (3) ◽  
pp. 465-472 ◽  
Author(s):  
Zvi Laron ◽  
Ariana Yed-Lekach ◽  
Sara Assa ◽  
Avivah Kowadlo-Silbergeld
Keyword(s):  
Heat Treatment ◽  
Growth Hormone ◽  
Electrophoretic Mobility ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Precipitation Reaction ◽  
Agar Gel ◽  
Immunological Properties ◽  
Haemagglutination Test ◽  
Precipitation Reactions

ABSTRACT Human, bovine and sheep (ovine) growth hormone (HGH, BGH and SGH) were heated in solution at temperatures between 60 and 100 °C. The electrophoretic mobility and immunological properties, such as precipitation reactions in agar gel and haemagglutination with antiserum to untreated hormone, were studied at different degrees of heating. It was found that heat progressively reduced the immunological properties of the growth hormone; however, human growth hormone was more resistant to heat treatment than the bovine and sheep growth hormone. HGH retained precipitation properties when heated at 100° C up to 30 minutes, and reacted in the haemagglutination test when heated at 100° C for less than 60 minutes. BGH and SGH clotted at 100° C. The precipitation reaction with antiserum to BGH disappeared when BGH or SGH was heated at 70° C for more than 10 minutes. Only a weak haemagglutination reaction was retained when BGH or SGH was heated at 80° C for 15 minutes.

Increased Availability of Human Growth Hormone: A Challenge for Health Economics

1988 ◽  
Vol 4 (4) ◽  
pp. 629-633 ◽  
Author(s):  
Kerstin Albertsson-Wikland ◽  
Agne Larsson
Keyword(s):  
Decision Making ◽  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Gh Treatment ◽  
Pituitary Glands ◽  
Rapid Transition ◽  
Dna Technology ◽  
Constant Prices ◽  
Hybrid Dna

Human growth hormone (GH) has until recently been prepared commercially from pituitary glands collected at autopsy. Availability has been limited and cost high, so the indications for GH treatment have had to be “tight.” Owing to recent development in hybrid DNA technology, the availability of GH has increased dramatically. At the same time, the manufacturers have maintained constant prices, so that treatment costs continue to influence decision making about its use. This rapid transition has generated an interesting change of strategy, which is outlined in this review.

Sign in / Sign up

Export Citation Format

Share Document